TICN3_PONAB
ID TICN3_PONAB Reviewed; 436 AA.
AC Q5RD69; Q5R5Q3;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Testican-3;
DE AltName: Full=SPARC/osteonectin, CWCV, and Kazal-like domains proteoglycan 3;
DE Flags: Precursor;
GN Name=SPOCK3;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May participate in diverse steps of neurogenesis. Inhibits
CC the processing of pro-matrix metalloproteinase 2 (MMP-2) by MT1-MMP and
CC MT3-MMP. May interfere with tumor invasion (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5RD69-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5RD69-2; Sequence=VSP_013634;
CC -!- TISSUE SPECIFICITY: Expressed in brain.
CC -!- PTM: Contains chondroitin sulfate and heparan sulfate O-linked
CC oligosaccharides. {ECO:0000250}.
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DR EMBL; CR858048; CAH90288.1; -; mRNA.
DR EMBL; CR860803; CAH92913.1; -; mRNA.
DR RefSeq; NP_001125130.1; NM_001131658.1. [Q5RD69-2]
DR RefSeq; NP_001128882.1; NM_001135410.1.
DR AlphaFoldDB; Q5RD69; -.
DR SMR; Q5RD69; -.
DR MEROPS; I31.007; -.
DR Ensembl; ENSPPYT00000017650; ENSPPYP00000016964; ENSPPYG00000015182. [Q5RD69-1]
DR Ensembl; ENSPPYT00000046963; ENSPPYP00000044038; ENSPPYG00000015182. [Q5RD69-1]
DR GeneID; 100172015; -.
DR GeneID; 100189814; -.
DR KEGG; pon:100172015; -.
DR CTD; 50859; -.
DR GeneTree; ENSGT00940000157828; -.
DR InParanoid; Q5RD69; -.
DR OrthoDB; 1235834at2759; -.
DR Proteomes; UP000001595; Chromosome 4.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005539; F:glycosaminoglycan binding; IEA:Ensembl.
DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0019800; P:peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan; IEA:Ensembl.
DR CDD; cd00191; TY; 1.
DR Gene3D; 4.10.800.10; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR019577; SPARC/Testican_Ca-bd-dom.
DR InterPro; IPR000716; Thyroglobulin_1.
DR InterPro; IPR036857; Thyroglobulin_1_sf.
DR Pfam; PF07648; Kazal_2; 1.
DR Pfam; PF10591; SPARC_Ca_bdg; 1.
DR Pfam; PF00086; Thyroglobulin_1; 1.
DR SMART; SM00280; KAZAL; 1.
DR SMART; SM00211; TY; 1.
DR SUPFAM; SSF100895; SSF100895; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF57610; SSF57610; 1.
DR PROSITE; PS51465; KAZAL_2; 1.
DR PROSITE; PS00484; THYROGLOBULIN_1_1; 1.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Heparan sulfate; Metalloenzyme inhibitor;
KW Metalloprotease inhibitor; Protease inhibitor; Proteoglycan;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..436
FT /note="Testican-3"
FT /id="PRO_0000026705"
FT DOMAIN 133..185
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 314..380
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT REGION 393..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..436
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 387
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 392
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT DISULFID 90..101
FT /evidence="ECO:0000250"
FT DISULFID 95..111
FT /evidence="ECO:0000250"
FT DISULFID 139..169
FT /evidence="ECO:0000250"
FT DISULFID 142..162
FT /evidence="ECO:0000250"
FT DISULFID 151..183
FT /evidence="ECO:0000250"
FT DISULFID 317..341
FT /evidence="ECO:0000250"
FT DISULFID 352..359
FT /evidence="ECO:0000250"
FT DISULFID 361..380
FT /evidence="ECO:0000250"
FT VAR_SEQ 64..66
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_013634"
SQ SEQUENCE 436 AA; 49457 MW; 04D57114FB24C389 CRC64;
MLKVSAVLCV CAAAWCSQSL AAAAAVAAAV GRSDGGNFLD DKQWLTTISQ YDKEVGQWNK
FRDEVEDDDF RTWSPGKPFD QALDPAKDPC LKMKCSRHKV CIAQDYQTAV CISHRRLTHR
MKEAGVDHRQ WRGPILSTCK QCPVVYPSPV CGSDGHTYSF QCKLEYQACV LGKQISVKCE
GHCPCPSDKP TSTSRNVKRA CSDLEFREVA NRLRDWFKAL HESGSQNKKT KTLLRPERSR
FDTSILPICK DSLGWMFNRL DTNYDLLLDQ SELRSIYLDK NEQCTKAFFN SCDTYKDSLI
SNNEWCYCFQ RQQDPPCQTE LSNIQKRQGV KKLLGQYIPL CDEDGYYKPT QCHGSVGQCW
CVDRYGNEVM GSRINGVADC AIDFEISGDF ASGDFHEWTD DEDDEDDIMN DEDEIEDDDE
DEGDDDDGGD DHDGYI
